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Grp78/BiP (hamster), (recombinant)

 
ADI-SPP-765-D 50 µg 213.00 USD
 
ADI-SPP-765-F 200 µg 479.00 USD
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Product Specification

Alternative Name:HspA5, Hsp70-5, Heat shock 70 kDa protein 5
 
MW:~78kDa
 
Source:Produced in E. coli.
 
UniProt ID:P07823
 
Formulation:Liquid. In 50mM Tris, pH 7.5, containing 150mM NaCl, 10% glycerol and 1mM DTT
 
Purity:≥80% (SDS-PAGE; Western blot)
 
Purity Detail:Purified by multi-step chromatography.
 
Applications:WB
 
Application Notes:Western blot control.
 
Shipping:Shipped on Dry Ice
 
Long Term Storage:-80°C
 
Scientific Background:Grp78, a 78 kDa glucose-regulated protein also known as BiP or immunoglobulin heavy chain binding protein, is a stress-response protein induced by agents or conditions that adversely affect endoplasmic reticulum (ER) function. This protein is essential for the proper glycosylation, folding and assembly of many membrane bound and secreted proteins. Grp78 is critical for maintenance of cell homeostasis and the prevention of apoptosis. Grp78 protein levels provide a reliable biomarker of hypoglycemia as well as serve a neuroprotective function in neurons exposed to glutamate and oxidative stress. Reduced Grp78 levels occur in the brains of Alzheimer’s Disease patients, and decreased Grp78 expression appears to be associated with missense mutations in the human presenilin-1 (PS1) gene. The induction of the Grp78 protein is associated with the development of drug-resistance to anti-tumor drugs.
 
SPP-765 SDS-PAGE
SDS-PAGE analysis: Lane 1: MWM, Lane 2: 0.5µg, Lane 3: 1µg, Lane 4: 2µg, Lane 5: 5µg of Recombinant Grp78 Hamster Protein.
SPP-765 WB1
Western Blot analysis: Lane 1: MW marker, Lane 2 and 3: Recombinant Grp78 Hamster Protein probed with anti-Recombinant Grp78 (Bip) pAb.
SPP-765 WB2
Western Blot analysis: Lane 1: MWM, Lane 2 and 3: Recombinant Grp78 Hamster Protein probed with Anti-KDEL (Grp78, Grp94) mAb.
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SPP-765 SDS-PAGE SPP-765 WB1 SPP-765 WB2

Product Literature References

Selection and identification of ligand peptides targeting a model of castrate-resistant osteogenic prostate cancer and their receptors: J. Mandelin, et al.; PNAS 112, 3776 (2015), Application(s): Western Blotting, Abstract; Full Text
Tumor imaging and targeting potential of an Hsp70-derived 14-mer peptide: M. Gehrmann, et al.; PLoS One 9, e105344 (2014), Abstract; Full Text
Differential protein expression during aging in ventricular myocardiumof Fischer 344 x Brown Norway hybrid rats: F. Witzmann, et al. ; Exp. Gerontol. 43, 909 (2008), Abstract;
Fingerprinting the circulating repertoire of antibodies from cancer patients: W. Arap, et al. ; Nat. Biotechnol. 21, 57 (2003), Application(s): WB , Abstract;
Coupling endoplasmic reticulum stress to the cell death program: role of the ER chaperone GRP78: D.E. Bredesen, et al. ; FEBS Lett. 514, 122 (2002), Application(s): WB , Abstract;
The dynamic role of GRP78/BiP in the coordination of mRNA translation with protein processing: C.O. Brostrom, et al. ; J. Biol. Chem. 274, 486 (1999), Application(s): WB , Abstract;

General Literature References

The critical roles of endoplasmic reticulum chaperones and unfolded protein response in tumorigenesis and anticancer therapies: B. Luo & A.S. Lee; Oncogene 32, 805 (2013), (Review), Abstract; Full Text
The critical role of GRP78 in physiologic and pathologic stress: K.T. Pfaffenbach & A.S. Lee; Curr. Opin. Cell Biol. 23, 150 (2011), (Review), Abstract; Full Text

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